NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1125450597|gb|OLD76867|]
View 

hypothetical protein AUF71_00050 [Gemmatimonadetes bacterium 13_1_20CM_69_52]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10888683)

uncharacterized member of the MBL fold metallo-hydrolase superfamily

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-266 1.81e-107

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


:

Pssm-ID: 293839  Cd Length: 252  Bit Score: 312.12  E-value: 1.81e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  14 HALEAGRQALDGGAMFGVVPKPLWQRRIPADERNRIPLALRCLLIEHDDGLVLVDTGLGNKEDAKFKDIYgvaneGQHGR 93
Cdd:cd16281     4 HSIEGGYFKLDGGAMFGVVPKPLWQKWYPADEDNRITLAMRCLLIETGGRNILIDTGIGDKQDPKFRSIY-----VQHSE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  94 TCLEDALAELGHAPQDVRWVINTHLHFDHAGGNTFRevveDGGGAIRVTFPRATHVVQRGELEFARHTNERTAASYLPPN 173
Cdd:cd16281    79 HSLLKSLARLGLSPEDITDVILTHLHFDHCGGATRA----DDDGLVELLFPNATYWVQKRHWEWALNPNPRERASFLPEN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 174 FEPVS----FTLVSG-EAAPLPGIRCLPTPGHVPFHQSVLVESAGERVCFLADLVPTAAHLPLPWIMGYDLEPLVTLESK 248
Cdd:cd16281   155 IEPLEesgrLKLIDGsDAELGPGIRFHLSDGHTPGQMLPEISTPGGTVVFAADLIPTSAHIPLPWVMGYDRRPLLTIEEK 234

                         250
                  ....*....|....*...
gi 1125450597 249 RRLYERAEAEGWLLFFEH 266
Cdd:cd16281   235 ERLLDEAVEEGGRLFFEH 252
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-266 1.81e-107

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293839  Cd Length: 252  Bit Score: 312.12  E-value: 1.81e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  14 HALEAGRQALDGGAMFGVVPKPLWQRRIPADERNRIPLALRCLLIEHDDGLVLVDTGLGNKEDAKFKDIYgvaneGQHGR 93
Cdd:cd16281     4 HSIEGGYFKLDGGAMFGVVPKPLWQKWYPADEDNRITLAMRCLLIETGGRNILIDTGIGDKQDPKFRSIY-----VQHSE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  94 TCLEDALAELGHAPQDVRWVINTHLHFDHAGGNTFRevveDGGGAIRVTFPRATHVVQRGELEFARHTNERTAASYLPPN 173
Cdd:cd16281    79 HSLLKSLARLGLSPEDITDVILTHLHFDHCGGATRA----DDDGLVELLFPNATYWVQKRHWEWALNPNPRERASFLPEN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 174 FEPVS----FTLVSG-EAAPLPGIRCLPTPGHVPFHQSVLVESAGERVCFLADLVPTAAHLPLPWIMGYDLEPLVTLESK 248
Cdd:cd16281   155 IEPLEesgrLKLIDGsDAELGPGIRFHLSDGHTPGQMLPEISTPGGTVVFAADLIPTSAHIPLPWVMGYDRRPLLTIEEK 234

                         250
                  ....*....|....*...
gi 1125450597 249 RRLYERAEAEGWLLFFEH 266
Cdd:cd16281   235 ERLLDEAVEEGGRLFFEH 252
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 44-286 1.98e-22

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 92.45  E-value: 1.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  44 DERNRIPLALRCLLIEHDDGLVLVDTGLGNKEDAKfkdiygvanegqhgrtcLEDALAELGhapQDVRWVINTHLHFDHA 123
Cdd:COG0491     6 GGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEA-----------------LLAALAALG---LDIKAVLLTHLHPDHV 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 124 GGNtfREVVEDGGgairvtfprATHVVQRGELEFARhtnERTAASYLPPNFEPVSFTLVSGEAAPL--PGIRCLPTPGHV 201
Cdd:COG0491    66 GGL--AALAEAFG---------APVYAHAAEAEALE---APAAGALFGREPVPPDRTLEDGDTLELggPGLEVIHTPGHT 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 202 PFHQSVLVEsaGERVCFLADLVPTAAHlplPWIMGYDLEPLVTLESKRRLYERaeaEGWLLFFEHDASVIAGRLGRDGKG 281
Cdd:COG0491   132 PGHVSFYVP--DEKVLFTGDALFSGGV---GRPDLPDGDLAQWLASLERLLAL---PPDLVIPGHGPPTTAEAIDYLEEL 203


                  ....*
gi 1125450597 282 FGLVE 286
Cdd:COG0491   204 LAALG 208
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 55-258 6.82e-19

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 81.83  E-value: 6.82e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597   55 CLLIEHDDGLVLVDTGLGNKEDakfkdiygvanegqhgrtcLEDALAELGhaPQDVRWVINTHLHFDHAGGNtfREVVED 134
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAED-------------------LLAELKKLG--PKKIDAIILTHGHPDHIGGL--PELLEA 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  135 GGGAIrvtfprathVVQRGELEFARHTNERTAASYLPPNFEPVSFTLVSGEAAPL--PGIRCLPTPGHVPFHQSVLVEsa 212
Cdd:smart00849  59 PGAPV---------YAPEGTAELLKDLLALLGELGAEAEPAPPDRTLKDGDELDLggGELEVIHTPGHTPGSIVLYLP-- 127

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1125450597  213 GERVCFLADLVPTAAHLPLpWIMGYDLEPLVTLESKRRLYERAEAE 258
Cdd:smart00849 128 EGKILFTGDLLFAGGDGRT-LVDGGDAAASDALESLLKLLKLLPKL 172
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
55-236 3.74e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 72.40  E-value: 3.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  55 CLLIEHDDGLVLVDTGLGNKEDAKFKdiygvanegqhgrtcledaLAELGHAPQDVRWVINTHLHFDHAGGNtfrEVVED 134
Cdd:pfam00753   8 SYLIEGGGGAVLIDTGGSAEAALLLL-------------------LAALGLGPKDIDAVILTHGHFDHIGGL---GELAE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 135 GGGAIRVTFPRATHVVQRGELEFARhtnERTAASYLPPNFEPVSFTLVSGEAAPLPGIRCLPTPGHVPFHQSVLVESAGE 214
Cdd:pfam00753  66 ATDVPVIVVAEEARELLDEELGLAA---SRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGG 142

                         170       180
                  ....*....|....*....|..
gi 1125450597 215 RVCFLADLVPTAAHLPLPWIMG 236
Cdd:pfam00753 143 KVLFTGDLLFAGEIGRLDLPLG 164
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-266 1.81e-107

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293839  Cd Length: 252  Bit Score: 312.12  E-value: 1.81e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  14 HALEAGRQALDGGAMFGVVPKPLWQRRIPADERNRIPLALRCLLIEHDDGLVLVDTGLGNKEDAKFKDIYgvaneGQHGR 93
Cdd:cd16281     4 HSIEGGYFKLDGGAMFGVVPKPLWQKWYPADEDNRITLAMRCLLIETGGRNILIDTGIGDKQDPKFRSIY-----VQHSE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  94 TCLEDALAELGHAPQDVRWVINTHLHFDHAGGNTFRevveDGGGAIRVTFPRATHVVQRGELEFARHTNERTAASYLPPN 173
Cdd:cd16281    79 HSLLKSLARLGLSPEDITDVILTHLHFDHCGGATRA----DDDGLVELLFPNATYWVQKRHWEWALNPNPRERASFLPEN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 174 FEPVS----FTLVSG-EAAPLPGIRCLPTPGHVPFHQSVLVESAGERVCFLADLVPTAAHLPLPWIMGYDLEPLVTLESK 248
Cdd:cd16281   155 IEPLEesgrLKLIDGsDAELGPGIRFHLSDGHTPGQMLPEISTPGGTVVFAADLIPTSAHIPLPWVMGYDRRPLLTIEEK 234

                         250
                  ....*....|....*...
gi 1125450597 249 RRLYERAEAEGWLLFFEH 266
Cdd:cd16281   235 ERLLDEAVEEGGRLFFEH 252
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 11-266 2.62e-72

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293814  Cd Length: 249  Bit Score: 222.52  E-value: 2.62e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  11 LTCHALEAGRQALDGGAMFGVVPKPLWQRRIPADERNRIPLALRCLLIEHDDGLVLVDTGLGN-KEDAKFKDIYGVANEG 89
Cdd:cd07728     1 IKLTWLDGGVTHLDGGAMFGVVPKPLWSKKYPANEKNQIELRTDPILIQYQGKNYLIDAGIGNgKLTEKQKRNFGVTEES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  90 QhgrtcLEDALAELGHAPQDVRWVINTHLHFDHAGGNTFREvvedgGGAIRVTFPRATHVVQRGELEFARHTNERTAASY 169
Cdd:cd07728    81 S-----IEESLAELGLTPEDIDYVLMTHLHFDHASGLTKVK-----GEQLVSVFPNATIYVSEIEWEEMRNPNIRSKNTY 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 170 LPPNFEPVS--FTLVSGEAAPLPGIRCLPTPGHVPFHQSVLVESAGERVCFLADLVPTAAHLPLPWIMGYDLEPLVTLES 247
Cdd:cd07728   151 WKENWEPIEdqVKTFSDEIEIVPGITMIHTGGHSDGHSIIEIEQGGETAIHMADLMPTHAHQNPLWVLAYDDYPMTSIEA 230

                         250
                  ....*....|....*....
gi 1125450597 248 KRRLYERAEAEGWLLFFEH 266
Cdd:cd07728   231 KEKWLKEGIKNNYWFTFYH 249
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 14-267 2.00e-52

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 171.24  E-value: 2.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  14 HALEAGRQALDGGAMFgvvpkplwqrRIPADERNRIPLALRCLLIEHDDGLVLVDTGLGNKEDAKFKDIYGVANEGQHGR 93
Cdd:cd07729     3 YALDYGTVTVDKSSLF----------YYGRGPGEPIDLPVYAYLIEHPEGTILVDTGFHPDAADDPGGLELAFPPGVTEE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  94 TCLEDALAELGHAPQDVRWVINTHLHFDHAGGNTFrevvedgggairvtFPRATHVVQRGELEFARHTNERTAASY---- 169
Cdd:cd07729    73 QTLEEQLARLGLDPEDIDYVILSHLHFDHAGGLDL--------------FPNATIIVQRAELEYATGPDPLAAGYYedvl 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 170 -LPPNFEPVSFTLVSGEAAPLPGIRCLPTPGHVPFHQSVLVESAGERVCFLADLVPTAAHL--PLPWIMGYDLEplVTLE 246
Cdd:cd07729   139 aLDDDLPGGRVRLVDGDYDLFPGVTLIPTPGHTPGHQSVLVRLPEGTVLLAGDAAYTYENLeeGRPPGINYDPE--AALA 216

                         250       260
                  ....*....|....*....|.
gi 1125450597 247 SKRRLYERAEAEGWLLFFEHD 267
Cdd:cd07729   217 SLERLKALAEREGARVIPGHD 237
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 6-266 1.76e-37

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 133.06  E-value: 1.76e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597   6 FRVGRLTCHALEAGRQALDGGAMFGVVPKP----LWQRRIPADernRIPLALRCLLIEHDDGLVLVDTGLGNkedakfkd 81
Cdd:cd07720     1 FKVGDFEVTALSDGTLPLPLDLLLGGAAPEaeaaLLAAFLPPD---PVETSVNAFLVRTGGRLILVDTGAGG-------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  82 iygvANEGQHGRtcLEDALAELGHAPQDVRWVINTHLHFDHAGGntfreVVEDGGgaiRVTFPRATHVVQRGELEF-ARH 160
Cdd:cd07720    70 ----LFGPTAGK--LLANLAAAGIDPEDIDDVLLTHLHPDHIGG-----LVDAGG---KPVFPNAEVHVSEAEWDFwLDD 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 161 TNERTAASYLPPNFEPVSFTL--------VSGEAAPLPGIRCLPTPGHVPFHQSVLVESAGERVCFLADLV-PTAAHLPL 231
Cdd:cd07720   136 ANAAKAPEGAKRFFDAARDRLrpyaaagrFEDGDEVLPGITAVPAPGHTPGHTGYRIESGGERLLIWGDIVhHPALQFAH 215

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1125450597 232 P-WIMGYDLEPLVTLESKRRLYERAEAEGWLLFFEH 266
Cdd:cd07720   216 PdWTIAFDVDPEQAAATRRRLLDRAAAEGLLVAGAH 251
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-263 3.57e-35

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 126.10  E-value: 3.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  48 RIPLALRCLLIEHDDGLVLVDTGLGN-KEDAkfkdiygVANEGQHGRTCLEDALAELGHAPQDVRWVINTHLHFDHAGGN 126
Cdd:cd16277     8 RIVELIHSWLVRTPGRTILVDTGIGNdKPRP-------GPPAFHNLNTPYLERLAAAGVRPEDVDYVLCTHLHVDHVGWN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 127 TFREvvedgGGAIRVTFPRATHVVQRGELEFARHTNERTAASylPPNFE----PV----SFTLVSGEAAPLPGIRCLPTP 198
Cdd:cd16277    81 TRLV-----DGRWVPTFPNARYLFSRAEYDHWSSPDAGGPPN--RGVFEdsvlPVieagLADLVDDDHEILDGIRLEPTP 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1125450597 199 GHVPFHQSVLVESAGERVCFLADLVPTAAHLPLP-WIMGYDLEPLVTLESKRRLYERAEAEGWLLF 263
Cdd:cd16277   154 GHTPGHVSVELESGGERALFTGDVMHHPIQVARPdWSSVFDEDPAQAAATRRRLLERAADTDTLLF 219
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 44-286 1.98e-22

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 92.45  E-value: 1.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  44 DERNRIPLALRCLLIEHDDGLVLVDTGLGNKEDAKfkdiygvanegqhgrtcLEDALAELGhapQDVRWVINTHLHFDHA 123
Cdd:COG0491     6 GGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEA-----------------LLAALAALG---LDIKAVLLTHLHPDHV 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 124 GGNtfREVVEDGGgairvtfprATHVVQRGELEFARhtnERTAASYLPPNFEPVSFTLVSGEAAPL--PGIRCLPTPGHV 201
Cdd:COG0491    66 GGL--AALAEAFG---------APVYAHAAEAEALE---APAAGALFGREPVPPDRTLEDGDTLELggPGLEVIHTPGHT 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 202 PFHQSVLVEsaGERVCFLADLVPTAAHlplPWIMGYDLEPLVTLESKRRLYERaeaEGWLLFFEHDASVIAGRLGRDGKG 281
Cdd:COG0491   132 PGHVSFYVP--DEKVLFTGDALFSGGV---GRPDLPDGDLAQWLASLERLLAL---PPDLVIPGHGPPTTAEAIDYLEEL 203


                  ....*
gi 1125450597 282 FGLVE 286
Cdd:COG0491   204 LAALG 208
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 55-258 6.82e-19

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 81.83  E-value: 6.82e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597   55 CLLIEHDDGLVLVDTGLGNKEDakfkdiygvanegqhgrtcLEDALAELGhaPQDVRWVINTHLHFDHAGGNtfREVVED 134
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAED-------------------LLAELKKLG--PKKIDAIILTHGHPDHIGGL--PELLEA 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  135 GGGAIrvtfprathVVQRGELEFARHTNERTAASYLPPNFEPVSFTLVSGEAAPL--PGIRCLPTPGHVPFHQSVLVEsa 212
Cdd:smart00849  59 PGAPV---------YAPEGTAELLKDLLALLGELGAEAEPAPPDRTLKDGDELDLggGELEVIHTPGHTPGSIVLYLP-- 127

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1125450597  213 GERVCFLADLVPTAAHLPLpWIMGYDLEPLVTLESKRRLYERAEAE 258
Cdd:smart00849 128 EGKILFTGDLLFAGGDGRT-LVDGGDAAASDALESLLKLLKLLPKL 172
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 50-266 2.12e-18

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 80.79  E-value: 2.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  50 PLALRCLLIEHDDG-LVLVDTGLGNkedakfkdiygvanegqhgrtcLEDALAELGHAPQDVRWVINTHLHFDHAGGNTf 128
Cdd:cd06262     7 PLQTNCYLVSDEEGeAILIDPGAGA----------------------LEKILEAIEELGLKIKAILLTHGHFDHIGGLA- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 129 rEVVEDgggairvtfPRATHVVQRGELEFARHTNERTAASYLPPNFEPVSFTLVSGEAAPLPG---IRCLPTPGHVPFHQ 205
Cdd:cd06262    64 -ELKEA---------PGAPVYIHEADAELLEDPELNLAFFGGGPLPPPEPDILLEDGDTIELGgleLEVIHTPGHTPGSV 133

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125450597 206 SVLVESagERVCFLADLVPTAAHLPLPWIMGYDLEplvTLESKRRLYERAEaEGWLLFFEH 266
Cdd:cd06262   134 CFYIEE--EGVLFTGDTLFAGSIGRTDLPGGDPEQ---LIESIKKLLLLLP-DDTVVYPGH 188
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 55-223 2.51e-17

uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Bacillus subtilis yflN protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 78.42  E-value: 2.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  55 CLLIEHDDGLVLVDTGLGNKEDAkfkdiygvanegqhgrtcLEDALAELGHAPQDVRWVINTHLHFDHAGGntFREVVED 134
Cdd:cd07721    13 AYLIEDDDGLTLIDTGLPGSAKR------------------ILKALRELGLSPKDIRRILLTHGHIDHIGS--LAALKEA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 135 GGgaIRVTFPRATHVVQRGELEFARHTNERTAASY---LPPNFEPVSFTLVSGEAAPL-PGIRCLPTPGHVPFHQSVLVE 210
Cdd:cd07721    73 PG--APVYAHEREAPYLEGEKPYPPPVRLGLLGLLsplLPVKPVPVDRTLEDGDTLDLaGGLRVIHTPGHTPGHISLYLE 150

                         170
                  ....*....|...
gi 1125450597 211 SagERVCFLADLV 223
Cdd:cd07721   151 E--DGVLIAGDAL 161
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 55-226 2.58e-17

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 78.01  E-value: 2.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  55 CLLIEHDDGLVLVDTGLGNkedakfkdiygvanegqhGRTCLEDALAELGHAPQDVRWVINTHLHFDHAGGNTFrevved 134
Cdd:cd07711    24 VTLIKDGGKNILVDTGTPW------------------DRDLLLKALAEHGLSPEDIDYVVLTHGHPDHIGNLNL------ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 135 gggairvtFPRATHVVqrGELEFARHtnertaasYLPPNFEPvsftlvSGEAAPLPGIRCLPTPGHVPFHQSVLVESAGE 214
Cdd:cd07711    80 --------FPNATVIV--GWDICGDS--------YDDHSLEE------GDGYEIDENVEVIPTPGHTPEDVSVLVETEKK 135

                         170
                  ....*....|...
gi 1125450597 215 RVCFLA-DLVPTA 226
Cdd:cd07711   136 GTVAVAgDLFERE 148
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 54-250 1.84e-16

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 76.92  E-value: 1.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  54 RCLLIEH-DDGLVLVDTGLGNKEDAKFKDIYGVANEGQHGRTCLEDA---LAELGHAPQDVRWVINTHLHFDHAGGntfr 129
Cdd:cd07730    24 LAFLIEHpTGGKILFDLGYRKDFEEYTPRVPERLYRTPVPLEVEEDVaeqLAAGGIDPEDIDAVILSHLHWDHIGG---- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 130 evVEDgggairvtFPRATHVVQRGELEFARHTNERTA--ASYLPPNFEPVSFTLVSGEAAP---LPGIRC---------- 194
Cdd:cd07730   100 --LSD--------FPNARLIVGPGAKEALRPPGYPSGflPELLPSDFEGRLVRWEEDDFLWvplGPFPRAldlfgdgsly 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 195 -LPTPGHVPFHQSVLV-ESAGERVCFLADLV--PTAAHLPLPWIMGYDLEPLVTLESKRR 250
Cdd:cd07730   170 lVDLPGHAPGHLGLLArTTSGTWVFLAGDAChhRIGLLRPSPLLPLPDLDDGADREAARE 229
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
55-236 3.74e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 72.40  E-value: 3.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  55 CLLIEHDDGLVLVDTGLGNKEDAKFKdiygvanegqhgrtcledaLAELGHAPQDVRWVINTHLHFDHAGGNtfrEVVED 134
Cdd:pfam00753   8 SYLIEGGGGAVLIDTGGSAEAALLLL-------------------LAALGLGPKDIDAVILTHGHFDHIGGL---GELAE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 135 GGGAIRVTFPRATHVVQRGELEFARhtnERTAASYLPPNFEPVSFTLVSGEAAPLPGIRCLPTPGHVPFHQSVLVESAGE 214
Cdd:pfam00753  66 ATDVPVIVVAEEARELLDEELGLAA---SRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGG 142

                         170       180
                  ....*....|....*....|..
gi 1125450597 215 RVCFLADLVPTAAHLPLPWIMG 236
Cdd:pfam00753 143 KVLFTGDLLFAGEIGRLDLPLG 164
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 55-172 4.49e-14

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 70.35  E-value: 4.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  55 CLLIEHDDGLVLVDTGLG--------NKEDAKFKDIYG-VANEGQhgrTCLEdALAELGHAPQDVRWVINTHLHFDHAGG 125
Cdd:cd07742    21 CLLVETDDGLVLVDTGFGladvadpkRRLGGPFRRLLRpRLDEDE---TAVR-QIEALGFDPSDVRHIVLTHLDLDHAGG 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1125450597 126 ntfrevVEDgggairvtFPRAT-HVVQRgELEFARHTNERTAASYLPP 172
Cdd:cd07742    97 ------LAD--------FPHATvHVHAA-ELDAATSPRTRYERRRYRP 129
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 55-221 7.48e-11

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 60.58  E-value: 7.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  55 CLLIEHDDGLVLVDTGLGNKEDAkfkdiygvanegqhgrtcLEDALAELGHAPQDVRWVINTHLHFDHAGgntfrevved 134
Cdd:cd07726    18 SYLLDGEGRPALIDTGPSSSVPR------------------LLAALEALGIAPEDVDYIILTHIHLDHAG---------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 135 GGGAIRVTFPRATHVV-QRGelefARHTN--ERTAAS----------YLPPNFEPVS----FTLVSGEAAPLPG--IRCL 195
Cdd:cd07726    70 GAGLLAEALPNAKVYVhPRG----ARHLIdpSKLWASaravygdeadRLGGEILPVPeervIVLEDGETLDLGGrtLEVI 145

                         170       180
                  ....*....|....*....|....*.
gi 1125450597 196 PTPGHVPFHQSVLVESagERVCFLAD 221
Cdd:cd07726   146 DTPGHAPHHLSFLDEE--SDGLFTGD 169
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 56-217 2.01e-09

Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup EVM-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 56.97  E-value: 2.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  56 LLIEHDDGLVLVDTGLGNKEDAKFKDIygvanegqhgrtcledalAELGHAPQDVRWVINTHLHFDHAGGNTfreVVEDG 135
Cdd:cd16315    25 ILITGDDGHVLIDSGTEEAAPLVLANI------------------RKLGFDPKDVRWLLSSHEHFDHVGGLA---ALQRA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 136 GGAIRVTFPRATHVVQRGELefarhTNERTAASYLPPnFEP--VSFTLVSGEAAPLPGIRCLP--TPGHVPFHQSVLVES 211
Cdd:cd16315    84 TGARVAASAAAAPVLESGKP-----APDDPQAGLHEP-FPPvrVDRIVEDGDTVALGSLRLTAhaTPGHTPGALSWTWRS 157


                  ....*.
gi 1125450597 212 AGERVC 217
Cdd:cd16315   158 CEGADC 163
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 49-254 1.04e-07

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 50.76  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  49 IPLALR---CLLIEHDDGLVLVDTGLGNKEDAKFkdiygvanegqhgrtcLEDALAELGHAPQDVRWVINTHLHFDHAGG 125
Cdd:cd07725     8 LPGPLGhvnVYLLRDGDETTLIDTGLATEEDAEA----------------LWEGLKELGLKPSDIDRVLLTHHHPDHIGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 126 -NTFREVvedggGAIRVtfprathvvqrgelefarhtnertaasyLPPNFEPVSftlvSGEAAPLPGIR--CLPTPGHVP 202
Cdd:cd07725    72 aGKLQEK-----SGATV----------------------------YILDVTPVK----DGDKIDLGGLRlkVIETPGHTP 114

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1125450597 203 FHqsVLVESAGERVCFLADLVptaahLP--LPWIMGYDLE---PLVT-LESKRRLYER 254
Cdd:cd07725   115 GH--IVLYDEDRRELFVGDAV-----LPkiTPNVSLWAVRvedPLGAyLESLDKLEKL 165
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 57-125 1.13e-07

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 51.82  E-value: 1.13e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125450597  57 LIEHDDGLVLVDTgLGNKEDAKFkdiygvanegqhgrtcLEDALAELGHAPQDVRWVINTHLHFDHAGG 125
Cdd:cd16280    26 AIDTGDGLILIDA-LNNNEAADL----------------IVDGLEKLGLDPADIKYILITHGHGDHYGG 77
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 53-202 3.37e-07

AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Pseudomonas Aeruginosa AIM-1, Serratia marcescens SMB-1, Erythrobacter vulgaris EVM-1, and Janthinobacterium lividum THIN-B. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of AIM-1-,SMB-1-, EVM-1-, THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 50.42  E-value: 3.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  53 LRCLLIEHDDGLVLVDTGLgnkedakfkdiygvanegQHGRTCLEDALAELGHAPQDVRWVINTHLHFDHAGGntFREVV 132
Cdd:cd16290    22 LSAVLITSPQGLILIDGAL------------------PQSAPQIEANIRALGFRLEDVKLILNSHAHFDHAGG--IAALQ 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1125450597 133 EDgGGAIRVTFPRATHVVQRGELefarhTNERTAASYLPPnFEPVS--FTLVSGEAAPLPG--IRCLPTPGHVP 202
Cdd:cd16290    82 RD-SGATVAASPAGAAALRSGGV-----DPDDPQAGAADP-FPPVAkvRVVADGEVVKLGPlaVTAHATPGHTP 148
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 97-223 4.65e-07

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 49.27  E-value: 4.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  97 EDALAELGHAPQDVRWVINTHLHFDHAGGNtfrEVVEDGGGAirvtfPRATHvvqRGELEFARHTNERTAASYL--PPNF 174
Cdd:cd16322    34 EKLLARFGTTGLTLLYILLTHAHFDHVGGV---ADLRRHPGA-----PVYLH---PDDLPLYEAADLGAKAFGLgiEPLP 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1125450597 175 EPVSFtLVSGEAAPLPGI--RCLPTPGHVPFHQSVLVESAGerVCFLADLV 223
Cdd:cd16322   103 PPDRL-LEDGQTLTLGGLefKVLHTPGHSPGHVCFYVEEEG--LLFSGDLL 150
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 53-202 5.87e-07

BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Bradyrhizobium diazoefficiens BJP-1, Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Caulobacter crescentus Mbl1b. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 49.63  E-value: 5.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  53 LRCLLIEHDDGLVLVDTGLGnkedakfkdiygvANEGQhgrtcLEDALAELGHAPQDVRWVINTHLHFDHAGGntFREVV 132
Cdd:cd16288    22 LASYLITTPQGLILIDTGLE-------------SSAPM-----IKANIRKLGFKPSDIKILLNSHAHLDHAGG--LAALK 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1125450597 133 EDGGGAIRVTFPRATHVVQRGELEFarHTNERTAAsylppnFEPVSF--TLVSGEAAPLPGIR--CLPTPGHVP 202
Cdd:cd16288    82 KLTGAKLMASAEDAALLASGGKSDF--HYGDDSLA------FPPVKVdrVLKDGDRVTLGGTTltAHLTPGHTR 147
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 61-126 2.23e-06

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 47.56  E-value: 2.23e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1125450597  61 DDGLVLVDTGLGnkedakfkdiYGVANEgqhgrtcLEDALAELGHAPqdVRWVINTHLHFDHAGGN 126
Cdd:cd16282    23 DDGVVVIDTGAS----------PRLARA-------LLAAIRKVTDKP--VRYVVNTHYHGDHTLGN 69
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 53-125 7.51e-06

metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B3 MBLs include Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Stenotrophomonas Maltophilia L1, and Bradyrhizobium diazoefficiens BJP-1, Serratia marcescens SMB-1, and Pseudomonas Aeruginosa AIM-1. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 46.38  E-value: 7.51e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125450597  53 LRCLLIEHDDGLVLVDTGLgnkedakfkdiygvanegQHGRTCLEDALAELGHAPQDVRWVINTHLHFDHAGG 125
Cdd:cd07708    22 LAAYLIVTPQGNILIDGDM------------------EQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGG 76
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 57-202 1.11e-05

Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of BJP-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 45.94  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  57 LIEHDDGLVLVDTGLgnkedakfkdiygvANEGQHgrtcLEDALAELGHAPQDVRWVINTHLHFDHAGGntFREVVEDGG 136
Cdd:cd16309    26 LITTPEGHILIDGAM--------------PQSTPL----IKDNIKKLGFDVKDVKYLLNTHAHFDHAGG--LAELKKATG 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125450597 137 gairvtfprATHVVQRGE---LEFARHTNERTAASYLPPnfEPVSFTLVSGEAAPLPGIRCLP--TPGHVP 202
Cdd:cd16309    86 ---------AQLVASAADkplLESGYVGSGDTKNLQFPP--VRVDRVIGDGDKVTLGGTTLTAhlTPGHSP 145
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 53-202 2.88e-05

Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of L1- and Pom-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293847  Cd Length: 239  Bit Score: 44.42  E-value: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  53 LRCLLIEHDDGLVLVDTGLGNKEDAkfkdiygvanegqhgrtcLEDALAELGHAPQDVRWVINTHLHFDHAGgnTFREvV 132
Cdd:cd16289    22 LTALLVKTPDGAVLLDGGMPQAADM------------------LLDNMRALGVAPGDLKLILHSHAHADHAG--PLAA-L 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1125450597 133 EDGGGAIRVTFPRATHVVQRGELEFARHTNERTaasylppnFEPVSF--TLVSGEAAPLPGIRCLP--TPGHVP 202
Cdd:cd16289    81 KRATGARVAANAESAVLLARGGSDDIHFGDGIT--------FPPVQAdrIVMDGEVVTLGGVTFTAhfTPGHTP 146
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 100-202 4.48e-05

Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 43.82  E-value: 4.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 100 LAELGHAPQDVRWVINTHLHFDHAGGNTfreVVEDGGGAIRVTFPRATHVVQRGelefarhTNERTAASYLP------PN 173
Cdd:cd16312    51 IEALGFRIEDVKLILNSHAHWDHAGGIA---ALQKASGATVAASAHGAQVLQSG-------TNGKDDPQYQAkpvvhvAK 120

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1125450597 174 FEPVSfTLVSGEAAPLPGIRCLP--TPGHVP 202
Cdd:cd16312   121 VAKVK-EVGEGDTLKVGPLRLTAhmTPGHTP 150
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 52-202 6.09e-05

Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup AIM-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 43.73  E-value: 6.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  52 ALRCLLIEHDDGLVLVDTGLgnkedakfkdiygvanegQHGRTCLEDALAELGHAPQDVRWVINTHLHFDHAGGntFREV 131
Cdd:cd16314    21 GISALLVTSDAGHILIDGGT------------------DKAAPLIEANIRALGFRPEDVRYIVSSHEHFDHAGG--IARL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125450597 132 VEDGGGAIRVTFPRAThVVQRGElefarhtNERTAASYLP-PNFEPVS--FTLVSGEA---APLpGIRCLPTPGHVP 202
Cdd:cd16314    81 QRATGAPVVAREPAAT-TLERGR-------SDRSDPQFLVvEKFPPVAsvQRIGDGEVlrvGPL-ALTAHATPGHTP 148
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 55-125 1.45e-04

uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YycJ protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 41.09  E-value: 1.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125450597  55 CLLIEHDDGLVLVDTGLGNKEdakfkdiygvanegqhgrtcLEDALAELGHAPQDVRWVINTHLHFDHAGG 125
Cdd:cd07733    11 CTYLETEDGKLLIDAGLSGRK--------------------ITGRLAEIGRDPEDIDAILVTHEHADHIKG 61
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 55-223 1.46e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 41.75  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  55 CLLIEHDDG-LVLVDTGLGNKEdakfkdiygvaneGQHGRTCLEDALAELghapqdvRWVINTHLHFDHAGGNTFrevve 133
Cdd:cd07743    10 IGVYVFGDKeALLIDSGLDEDA-------------GRKIRKILEELGWKL-------KAIINTHSHADHIGGNAY----- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 134 dgggairvtFPRATHVV---QRGELEFARHTNERTaaSYL---PPNFE-----------PVSFTLVSGEAAPLP-GIRCL 195
Cdd:cd07743    65 ---------LQKKTGCKvyaPKIEKAFIENPLLEP--SYLggaYPPKElrnkflmakpsKVDDIIEEGELELGGvGLEII 133

                         170       180
                  ....*....|....*....|....*...
gi 1125450597 196 PTPGHVPFHQSVLVEsagERVCFLADLV 223
Cdd:cd07743   134 PLPGHSFGQIGILTP---DGVLFAGDAL 158
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 54-254 2.97e-04

uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 40.69  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  54 RCLLIEHDDGLVLVDTGLGNKEdakfkdiygvanegqhgrtcLEDALAELGHAPQDVrwvINTHLHFDHAGGNT-FREVV 132
Cdd:cd07712    10 NIYLLRGRDRALLIDTGLGIGD--------------------LKEYVRTLTDLPLLV---VATHGHFDHIGGLHeFEEVY 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 133 --EDGGGAIRVTFPRATHvvqrgelefarhtnERTAASYLPPNFEPVSfTLVSGEAAPLpGIRCLP---TPGHVPFHQSV 207
Cdd:cd07712    67 vhPADAEILAAPDNFETL--------------TWDAATYSVPPAGPTL-PLRDGDVIDL-GDRQLEvihTPGHTPGSIAL 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1125450597 208 LveSAGERVCFLADLVPTAahlplPWIM-GYDLEPLVTLESKRRLYER 254
Cdd:cd07712   131 L--DRANRLLFSGDVVYDG-----PLIMdLPHSDLDDYLASLEKLSKL 171
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 53-210 4.04e-04

Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of GOB-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 40.92  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  53 LRCLLIEHDDGLVLVDTGLGNKEdakfkdiygvanegqhgrTCLEDALAELGHAPQDVRWVINTHLHFDHAGGntFREVV 132
Cdd:cd16308    22 LACYLIVTPKGNILINTGLAESV------------------PLIKKNIQALGFKFKDIKILLTTQAHYDHVGA--MAAIK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 133 EDGGGAIRVTFPRATHVVQRGELEFarhtnERTAASYLppnFEPVSF--TLVSGEAAPLPG--IRCLPTPGHVPFHQSVL 208
Cdd:cd16308    82 QQTGAKMMVDEKDAKVLADGGKSDY-----EMGGYGST---FAPVKAdkLLHDGDTIKLGGtkLTLLHHPGHTKGSCSFL 153


                  ..
gi 1125450597 209 VE 210
Cdd:cd16308   154 FD 155
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 57-202 4.48e-04

Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of Mbl1b-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293868  Cd Length: 252  Bit Score: 40.90  E-value: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  57 LIEHDDGLVLVDTGLgnKEDAKFkdiygvanegqhgrtcLEDALAELGHAPQDVRWVINTHLHFDHAGGntFREVVEDGG 136
Cdd:cd16310    26 LITSNHGAILLDGGL--EENAAL----------------IEQNIKALGFKLSDIKIIINTHAHYDHAGG--LAQLKADTG 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 137 GAIRVTFPRAThvvqrgELEFARHTNERTaasYLPPNFEPVSF--TLVSGEAAPLPGIRCLP--TPGHVP 202
Cdd:cd16310    86 AKLWASRGDRP------ALEAGKHIGDNI---TQPAPFPAVKVdrILGDGEKIKLGDITLTAtlTPGHTK 146
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 102-125 1.03e-03

SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of SMB-1- and THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 39.85  E-value: 1.03e-03
                          10        20
                  ....*....|....*....|....
gi 1125450597 102 ELGHAPQDVRWVINTHLHFDHAGG 125
Cdd:cd16313    53 QLGFKLEDVKYILSSHDHWDHAGG 76
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 65-223 1.21e-03

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 39.05  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  65 VLVDTGLGNKEdakfkdiYgvanegqhgRTCLEDALAELGHAPqdVRWVINTHLHFDHAGGntFREVVED-GGGAIRVT- 142
Cdd:cd07722    30 ILIDTGEGRPS-------Y---------IPLLKSVLDSEGNAT--ISDILLTHWHHDHVGG--LPDVLDLlRGPSPRVYk 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 143 FPRATHVVQRGELEFARHtnertaasYLPPN--FEPVSFTLvsgeaaplpgiRCLPTPGHVPFHQSVLVESagERVCFLA 220
Cdd:cd07722    90 FPRPEEDEDPDEDGGDIH--------DLQDGqvFKVEGATL-----------RVIHTPGHTTDHVCFLLEE--ENALFTG 148


                  ...
gi 1125450597 221 DLV 223
Cdd:cd07722   149 DCV 151
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 55-239 1.28e-03

Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism];


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 39.49  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  55 CLLIEHDDGLVLVDTGLGnkedakFKDIygvanegqhgrtcledaLAELGHAPQDVRWVINTHLHFDHAGG-NTFREVVe 133
Cdd:COG1235    37 SILVEADGTRLLIDAGPD------LREQ-----------------LLRLGLDPSKIDAILLTHEHADHIAGlDDLRPRY- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597 134 dGGGAIRVTFPRATHVVQRGELEFARHTnertaasyLPPNFEPVSFTLvsGEAAPLPGIRCLPTPGHVPFHQSV--LVES 211
Cdd:COG1235    93 -GPNPIPVYATPGTLEALERRFPYLFAP--------YPGKLEFHEIEP--GEPFEIGGLTVTPFPVPHDAGDPVgyRIED 161

                         170       180
                  ....*....|....*....|....*...
gi 1125450597 212 AGERVCFLADLVPTAAHLpLPWIMGYDL 239
Cdd:COG1235   162 GGKKLAYATDTGYIPEEV-LELLRGADL 188
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 98-200 2.10e-03

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 38.21  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125450597  98 DALAELGHapqDVRWVINTHLHFDHAGGNtfREVVEDGG-----GAIRVTFPRATHVVQRGElefarhtnertaasylpp 172
Cdd:cd07723    35 AALEKNGL---TLTAILTTHHHWDHTGGN--AELKALFPdapvyGPAEDRIPGLDHPVKDGD------------------ 91

                          90       100
                  ....*....|....*....|....*...
gi 1125450597 173 nfepvSFTLVSGEaaplpgIRCLPTPGH 200
Cdd:cd07723    92 -----EIKLGGLE------VKVLHTPGH 108
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 53-125 4.02e-03

Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of THIN-B2-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293869  Cd Length: 257  Bit Score: 38.04  E-value: 4.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125450597  53 LRCLLIEHDDGLVLVDTGLgnKEDAKfKDIYGVAnegqhgrtcledalaELGHAPQDVRWVINTHLHFDHAGG 125
Cdd:cd16311    22 LSSVLVTSPQGHVLVDGGL--PESAP-KIIANIE---------------ALGFRIEDVKLILNSHGHIDHAGG 76
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH